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Database: UniProt
Entry: A0A0J6YLW1_COCIT
LinkDB: A0A0J6YLW1_COCIT
Original site: A0A0J6YLW1_COCIT 
ID   A0A0J6YLW1_COCIT        Unreviewed;       422 AA.
AC   A0A0J6YLW1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=26S protease regulatory subunit 6B {ECO:0000313|EMBL:KMP07913.1};
GN   ORFNames=CIRG_07594 {ECO:0000313|EMBL:KMP07913.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP07913.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; DS028097; KMP07913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YLW1; -.
DR   STRING; 404692.A0A0J6YLW1; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:KMP07913.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KMP07913.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT   DOMAIN          199..338
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          59..86
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   422 AA;  47214 MW;  004D7C22675C6B2A CRC64;
     MGDAIVETPV NVLAPPLKAT PAEAIPDIEP LEGWGTDDAD EYTTLKRLQR HLEYINLQEE
     YIKDEQRSLK RELVRAQEEI KRIQSVPLVI GQFMEAIDQN TGIVQSSTGS NYVVRILSTL
     DREKLKPSSS VALHRHSNAL VDILPPEADS SIAMLGAHEK PDVTYADVGG LDMQKQEIRE
     AVELPLTHFD LYKQIGIDPP RGVLLYGPPG TGKTMLVKAV ANSTTANFIR VVGSEFVQKY
     LGEGPRMVRD VFRMARENSP AIIFIDEIDA IATKRFDAQT GADREVQRIL LELLNQMDGF
     DQTSNVKVIM ATNRADTLDP ALLRPGRLDR KIEFPSLRDR RERRLIFTTI ASKMSLSPEV
     DLDSLIVRND PLSGAVIAAI MQEAGLRAVR KNRYNIIQSD LEDAYSSQVK SGQDADKFDF
     YR
//
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